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3.4.23.39: plasmepsin II

This is an abbreviated version!
For detailed information about plasmepsin II, go to the full flat file.

Word Map on EC 3.4.23.39

Reaction

Hydrolysis of the bonds linking certain hydrophobic residues in hemoglobin or globin. Also cleaves the small molecule substrates such as Ala-Leu-Glu-Arg-Thr-Phe!Phe(NO2)-Ser-Phe-Pro-Thr =

Synonyms

AH II, aspartic hemoglobinase II, malarial aspartic protease, PFAPD, pfpm2, plasmepsin 2, plasmepsin II, PLm II, PLMII, PM II, PMII, PSM2

ECTree

     3 Hydrolases
         3.4 Acting on peptide bonds (peptidases)
             3.4.23 Aspartic endopeptidases
                3.4.23.39 plasmepsin II

General Information

General Information on EC 3.4.23.39 - plasmepsin II

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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
-
multiple plasmepsin knockout mutants lacking plasmepsins I-III and I-IV, respectively show a significant increased parasite susceptibility to cyteine protease inhibitors. A ninefold increase in the potency of the calpain inhibitor N-acetyl-leucinyl-leucinyl-norleucinal (ALLN) against parasites lacking all four plasmepsins (I-IV) is observed. It is hypothesized that plasmepsins and some cysteine proteases play redundant or complementary roles in the digestive vacuole and that the absence of all plasmepsins (I-IV) renders these parasites highly susceptible to N-acetyl-leucinyl-leucinyl-norleucinal-mediated inhibition of falcipains
physiological function
enzyme overexpression fails to change the susceptibility of Plasmodium falciparum to artemisinin, chloroquine and piperaquine